STRUCTURAL CHARACTERIZATION OF THE ATP-DEPENDENT DIMER FORM OF BACTERIAL SEGEGRA

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 在大肠杆菌中，Min系统(Mind，Mind和My)通过将Z环组装限制在中间细胞位置来空间调节细胞分裂。心灵是一个膜相关的ATPase，它是一个更大的ATPase家族的一部分。这些蛋白包括PAR蛋白和固氮酶铁蛋白家族。在FtsZ(微管蛋白同源物)之后，Mind是细胞分裂机制中最保守的组成部分。在ATP存在的情况下，Mind二聚化，结合到膜上，并招募Minc。心灵与Minc捆绑在一起，抑制细胞分裂。与它们的功能一致，MIN系统被发现在细胞极点之间振荡。Mind ATPase对Min蛋白的振荡至关重要。有人提出，这种行为掩盖了潜在的分裂位点，并将细胞分裂机制定位于中细胞。显然，对活跃的依赖于三磷酸腺苷的二聚体的结构的确定将为深入了解这一重要分子的功能作用提供重要的见解。以前的Mind相关蛋白结构都是古生代的单体。因此，与生物相关的依赖于ATP的二聚体结构尚不清楚。这些古生菌蛋白与大肠杆菌蛋白几乎没有同源性(

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In E. coli the Min system (MinD, MinD and MinE) spatially regulates cell division by restricting Z ring assembly to a midcell location. MinD is a membrane associated ATPase, which is part of a larger family of ATPases. These include the family of Par proteins and nitrogenase iron proteins. After FtsZ (a tubulin homologue), MinD is the most highly conserved component of the cell division machinery. In the presence of ATP, MinD dimerizes, binds to the membrane and recruits MinC. MinD binds to MinC inhibiting cell division. Consistent with their function, the min system has been found to oscillate from cell pole to cell pole. The MinD ATPase is critical to the oscillation of the Min proteins. It has been proposed that this behavior masks potential division sites and localizes the cell division machinery to midcell. Clearly the determination of the structure of the active ATP-dependent dimer form of MinD will provide significant insight into the functional role of this important molecule. Previous structures of MinD related proteins are monomers from Archaea sp. Therefore the biologically relevant ATP dependent dimer structure is unknown. These archaeal proteins have little homology to the E. coli protein (